More handpicked essays just for you.
Enzymes and their functions
Functions of enzymes in medicine and industries
Functions of enzymes in medicine and industries
Don’t take our word for it - see why 10 million students trust us with their essay needs.
An enzyme can be defined as a protein that acts as a catalyst in a biological system. It increases the rate of reaction by decreasing the activation energy. The catalytic power and specificity of an enzyme can be altered by the binding of certain molecules. These molecules are referred to as inhibitors. An inhibitor works to prevent the formation, or to cause the breakdown of an enzyme-substrate compound. There are two categories of inhibitors. The first being irreversible inhibitors, and the second being reversible inhibitors. Irreversible inhibitors tend to be more tightly bound, covalently or noncovalently (mostly covalently), to the enzyme than reversible inhibitors, which tend to dissociate more rapidly from the enzyme. Reversible inhibitors can be subdivided into three groups: competitive, uncompetitive, and noncompetitive. Competitive inhibition occurs whenever the inhibitor (which resembles the substrate) binds at the active site of an enzyme. The inhibitor positioning itself at the active site, blocks the chance of a substrate binding to the active site of the enzyme. The binding of a competitive inhibitor to the active site, reduces the …show more content…
catalysis rate, due to the decrease in enzyme-substrate compounds. To overcome competitive inhibition, the solution is to increase the substrate concentration. Increasing the substrate concentration, the substrate will out compete the inhibitor’s concentration, thus reducing the possibility of the inhibitor binding to the active site. An enzyme in the competitive inhibitor scenario can bind either a substrate or inhibitor, but not both concurrently. Uncompetitive inhibition occurs whenever the inhibitor binds the enzyme-substrate compound. Unlike in competitive inhibition, an uncompetitive inhibitor does not bind to the active site. It also cannot be overcome by increasing the concentration of the substrate. Noncompetitive inhibition occurs when both the inhibitor and substrate bind to the enzyme, but at different locations on the enzyme. A noncompetitive inhibition has the ability to bind either a free floating enzyme, or an enzyme substrate compound. It works by reducing the concentration of an enzyme. By reducing the amount of enzyme, it results in a reduction of the enzyme-substrate compound concentration. Also, unlike competitive inhibition, noncompetitive inhibition cannot be overcome by increasing the substrate concentration. The Michaelis-Menten plot is used to show the kinetic aspect of an enzyme.
On a Michaelis-Menten plot, the presence of a competitive inhibitor results in a change of the Km value, but not the Vmax value. With an Uncompetitive inhibitor both the Km and the Vmax are decreased. A Noncompetitive inhibitor decreases the value of Vmax, but doesn’t affect Km. The Lineweaver-Burk plot is the reciprocal of the Michaelis-Menten plot. A competitive inhibitor affects a Lineweaver-Burk plot by causing a right shift in the x-axis. With an uncompetitive inhibitor, the shift occurs along both the x-axis and y-axis. The x-axis is shifted to the left, and the y-axis is shift up. A noncompetitive inhibitor on a Lineweaver-Burk plot will have a slope that in shifted higher along the
y-axis. From my results, I determined the type of inhibitor present to be a competitive inhibitor. I came to this conclusion after reviewing both the Michaelis-Menten and Lineweaver-Burk plots. On the Michaelis-Menten plot, the results show a change in the Km, but the Vmax value remained constant. On the Lineweaver-Burk plot, there is a right shift along the x-axis, which correlates with the results of a competitive inhibitor being present.
In the lab, Inhibiting the Action of Catechol Oxidase we had to investigate what type of enzyme inhibition occurs when an inhibitor is added. Catechol oxidase is an enzyme in plants that creates benzoquinone.Benzoquinone is a substance that is toxic to bacteria. It is brown and is the reason fruit turns brown. Now, there are two types of inhibitors, the competitive inhibitor and non-competitive inhibitor. For an enzyme reaction to occur a substrate has to bind or fit into the active site of the enzyme. In competitive inhibition there is a substrate and an inhibitor present, both compete to bind to the active site. If the competitive inhibitor binds to the active site it stops the reaction. A noncompetitive inhibitor binds to another region
The experiment of Diels-Alder reactions, in particular the furan and maleic anhydride as used in my experiment, observed the exo product as oppose to the exo product. This shows the tendency for the stereochemistry of the Diels-Alder to yield an exo product in preference to the endo product. To determine the stereochemistry, a melt temperature of the product was taken and compared to literature values. The melt temperature for the product was roughly around 113oC, corresponding to the exo Diels-Alder product of furan and maleic anhydride. When compared to the class data of melting ranges, the melting temperature from the reaction was relatively consistent to the majority. Based off this, the assumption can be made that the Diels-Alder prefers
Overall, as the concentration of the substrate increases, the enzyme activity increases up to a 70% of solution, where the enzyme activity starts to level off. The curve is polynomial because of the fact that the enzyme activity exponentially increases as the concentration of substrate increase; additional evidence for this is the fact that the gradient graph is constantly changing. The polynomial curve is shown because until 70% (the saturation point); this is because there are more casein substrate molecules that can successfully collide with the renin enzyme molecule, therefore increasing the rate of reaction.
When this substrate fits into the active site, it forms an enzyme-substrate complex. This means that an enzyme is specific. The bonds that hold enzymes together are quite weak and so are easily broken by conditions that are very different when compared with their optimum conditions. When these bonds are broken the enzyme, along with the active site, is deformed, thus deactivating the enzyme. This is known as a denatured enzyme.
Background information:. Enzyme Enzymes are protein molecules that act as the biological catalysts. A Catalyst is a molecule which can speed up chemical reactions but remains unchanged at the end of the reaction. Enzymes catalyze most of the metabolic reactions that take place within a living organism. They speed up the metabolic reactions by lowering the amount of energy.
Competition is everywhere in our daily lives. It begins from the day we are born until the day we die. Competition is just another word for challenge.
Enzymes are biological catalysts - catalysts are substances that increase the rate of chemical reactions without being altered itself. Enzymes are also proteins that fold into complex shapes that allow smaller molecules to fit into them. The place where these substrate molecules fit is called the active site. The active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of residues that form temporary bonds with the substrate and residues that catalyse a reaction of that substrate. (Clark, 2016)
An enzyme is a catalysis and catalysis s substance that increases the rate of a chemical reaction without itself going through a permanent chemical change. In this lab we will discover exactly how the substrate connects with the active site. The main substance we use throughout this lab is peroxidase a eukaryotic organelle from plant tissues. Once there is a color change we test that using a spectrophotometer. Introduction
Enzymes have the ability to act on a small group of chemically similar substances. Enzymes are very specific, in the sense that each enzyme is limited to interact with only one set of reactants; the reactants are referred to as substrates. Substrates of an enzyme are the chemicals altered by enzyme-catalysed reactions. The extreme specific nature of enzymes are because of the complicated three-dimensional shape, which is due to the particular way the amino acid chain of proteins folds.
Enzymes are types of proteins that work as a substance to help speed up a chemical reaction (Madar & Windelspecht, 104). There are three factors that help enzyme activity increase in speed. The three factors that speed up the activity of enzymes are concentration, an increase in temperature, and a preferred pH environment. Whether or not the reaction continues to move forward is not up to the enzyme, instead the reaction is dependent on a reaction’s free energy. These enzymatic reactions have reactants referred to as substrates. Enzymes do much more than create substrates; enzymes actually work with the substrate in a reaction (Madar &Windelspecht, 106). For reactions in a cell it is important that a specific enzyme is present during the process. For example, lactase must be able to collaborate with lactose in order to break it down (Madar & Windelspecht, 105).
Zanele muholi is a visual photographer and an activist of Black lesbian community. Using photography she addresses the challenges being faced by black lesbian, gay, bisexual, transgender and intersex people in both townships and communities. These people are vulnerable and they cannot speak for themselves but, through the pictures they are able to raise their concerns. Most of Zanele pictures are in black and white because according to her, one is able to concentrate in the message than the colour. This essay will therefore, discuss the significance of Zanele’s choice of photographic portraits as a medium to raise the concerns of LGBI community by using some of her images.
Enzymes have been used in research, mainly because of their ability to facilitate reactions without being changed themselves as well as their ability to speed up these reactions, which would otherwise take a much longer period of time to complete. And it is these two features that compel me to conduct further research into the applications of enzymes.
Enzymes are protein molecules that are made by organisms to catalyze reactions. Typically, enzymes speeds up the rate of the reaction within cells. Enzymes are primarily important to living organisms because it helps with metabolism and the digestive system. For example, enzymes can break larger molecules into smaller molecules to help the body absorb the smaller pieces faster. In addition, some enzyme molecules bind molecules together. However, the initial purpose of the enzyme is to speed up reactions for a certain reason because they are “highly selective catalysts” (Castro J. 2014). In other words, an enzyme is a catalyst, which is a substance that increases the rate of a reaction without undergoing changes. Moreover, enzymes work with
Heinrich Heine’s famously unfinished work, “The Rabbi of Bacherach,” offers an insightful look into the social history of Germany as well as into Heine’s own life. The skillful writer recounts the tale of a rabbi and his wife, who are forced to flee their native town of Bacherach after an anti-Semitic attack on their family. Thus, the work touches upon the social issues that plagued German society, and it offers a powerfully direct assessment of their incidence in history. However, the story was never completed and remains just a nascent, unpolished fragment.
The Perceived Demand Curve for a Perfect Competitor and Monopolist (Principle of Microeconomics, 2016). A perfectly competitive firm (a) has multiple firms competing against it, making the same product. Therefore the market sets the equilibrium price and the firm must accept it. The firm can produce as many products as it can afford to at the equilibrium price. However, a monopolist firm (b) can either cut or raise production to influence the price of their products or service. Therefore, giving it the ability to make substantial products at the cost of the consumers. However, not all monopolies are bad and some are even supported by the